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Título: | Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. |
Autor(es): | Breguez, Gustavo Silveira Neves, Leandro Xavier Rúbio, Karina Taciana Santos Freitas, Lorran Miranda Andrade de Faria, Gabriela de Oliveira Isoldi, Mauro César Borges, William de Castro Andrade, Milton Hércules Guerra de |
Palavras-chave: | Proline rich-peptides Label-free shotgun |
Data do documento: | 2016 |
Referência: | BREGUEZ, G. S. et al. Exposure of cultured fibroblasts to the peptide PR-11 for the identification of induced proteome alterations and discovery of novel potential ligands. Biochimica et Biophysica Acta. Proteins and Proteomics, v. 1864, p. 1775-1786, 2016.Disponível em: <http://www.sciencedirect.com/science/article/pii/S157096391630200X?via%3Dihub>. Acesso em: 15 set. 2017. |
Resumo: | The PR-11 peptide corresponds to the N-terminal and active region of the endogenously synthesized PR-39 molecule, of porcine origin. It is known to possess various biological effects including antimicrobial properties, angiogenic and anti-inflammatory activities. Apart from its reported activity as a proteasome inhibitor, a more comprehensive understanding of its function, at the molecular level, is still lacking. In this study, we used a label-free shotgun strategy to evaluate the proteomic alterations caused by exposure of cultured fibroblasts to the peptide PR-11. This approach revealed that more than half of the identified moleculeswere related to signalling, transcription and translation. Proteins directly associated to regulation of angiogenesis and interaction with the hypoxia-inducible factor 1-α (HIF-1α) were significantly altered. In addition, at least three differentially expressed molecules of the NF-κB pathway were detected, suggesting an anti-inflammatory property of PR-11. At last, we demonstrated novel potential ligands of PR-11, through its immobilization for affinity chromatography. Among the elutedmolecules, gC1qR, a known complement receptor, appearedmarkedly enriched. This provided preliminary evidence of a PR-11 ligand possibly involved in the internalization of this peptide. Altogether, our findings contributed to a better understanding of the cellular pathways affected by PR-39 derived molecules. |
URI: | http://www.repositorio.ufop.br/handle/123456789/9226 |
DOI: | https://doi.org/10.1016/j.bbapap.2016.09.017 |
ISSN: | 1570-9639 |
Licença: | O periódico Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 4210811289890. |
Aparece nas coleções: | DECBI - Artigos publicados em periódicos |
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Arquivo | Descrição | Tamanho | Formato | |
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ARTIGO_ExposureCulturedFibroblast.pdf | 910,55 kB | Adobe PDF | Visualizar/Abrir |
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